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Reviewed, UniProtKB/Swiss-Prot Q09131 (PPAF_SOYBN)

Last modified February 9, 2010. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Purple acid phosphatase
    EC=3.1.3.2
Alternative name(s):
    Zinc(II) purple acid phosphatase
Gene names
Name: PAP
OrganismGlycine max (Soybean)
Taxonomic identifier3847 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Glycine

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Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate. Ref.1 Ref.2

Cofactor

Binds 1 iron ion per subunit. Ref.1 Ref.2

Binds 1 zinc ion per subunit. Can also use manganese, copper and magnesium ions. Ref.1 Ref.2

Subunit structure

Homodimer; disulfide-linked By similarity. Ref.2 UniProtKB P80366

Subcellular location

Secreted Ref.2.

Sequence similarities

Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.

Biophysicochemical properties

Absorption:

Abs(max)=550 nm

Kinetic parameters:

KM=8 µM for p-NPP (at pH 5.5 and 25 degrees Celsius) Ref.1

KM=5 µM for ATP (at pH 5.5 and 25 degrees Celsius) Ref.1

KM=6 µM for ADP (at pH 5.5 and 25 degrees Celsius) Ref.1

KM=9 µM for AMP (at pH 5.5 and 25 degrees Celsius) Ref.1

KM=9 µM for pyrophosphate (at pH 5.5 and 25 degrees Celsius) Ref.1

KM=30 µM for beta-glycerophosphate (at pH 5.5 and 25 degrees Celsius) Ref.1

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Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandIron
Metal-binding
Zinc
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular componentextracellular space Ref.1

Inferred from direct assay. Source: UniProtKB

   Molecular functionacid phosphatase activity Ref.1

Inferred from direct assay. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

manganese ion binding Ref.1

Inferred from direct assay. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Ref.2
Chain31 – 464434Purple acid phosphatase Ref.2
PRO_0000043380

Regions

Region350 – 3523Substrate binding By similarity

Sites

Active site3231Proton donor By similarity UniProtKB P80366
Metal binding1621Iron By similarity UniProtKB P80366
Metal binding1911Iron By similarity UniProtKB P80366
Metal binding1911Zinc By similarity UniProtKB P80366
Metal binding1941Iron By similarity UniProtKB P80366
Metal binding2281Zinc By similarity UniProtKB P80366
Metal binding3131Zinc By similarity UniProtKB P80366
Metal binding3501Zinc By similarity UniProtKB P80366
Metal binding3521Iron By similarity UniProtKB P80366
Binding site2281Substrate By similarity

Amino acid modifications

Glycosylation1081N-linked (GlcNAc...) Potential
Glycosylation1361N-linked (GlcNAc...) Potential
Glycosylation1701N-linked (GlcNAc...) Potential
Glycosylation3011N-linked (GlcNAc...) Potential
Glycosylation3981N-linked (GlcNAc...) Potential
Glycosylation4231N-linked (GlcNAc...) Potential
Disulfide bond372Interchain By similarity UniProtKB P80366

Experimental info

Sequence conflict351T → A AA sequence Ref.2
Sequence conflict471V → R AA sequence Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q09131-1 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 83BBAD593BEB01F5

FASTA46453,027
        10         20         30         40         50         60 
MGVVEGLLAL ALVLSACVMC NGGSSSPFIR KVEKTVDMPL DSDVFAVPPG YNAPQQVHIT 

        70         80         90        100        110        120 
QGDLVGKAVI VSWVTVDEPG SSEVHYWSEN SDKKKIAEGK LVTYRFFNYS SGFIHHTTIR 

       130        140        150        160        170        180 
NLEYKTKYYY EVGLGNTTRQ FWFVTPPEIG PDVPYTFGLI GDLGQSFDSN KTLSHYELNP 

       190        200        210        220        230        240 
RKGQTVLFVG DLSYADNYPN HDNIRWDSWG RFTERSVAYQ PWIWTAGNHE NHFAPEIGET 

       250        260        270        280        290        300 
VPFKPYTHRY HVPYKASQST SPFWYSIKRA SAHIIVLASY SAYGKYTPQY KWLEKELPKV 

       310        320        330        340        350        360 
NRTETPWLIV LMHSPWYNSY NYHYMEGETM RVMYEPWFVQ YKVDVVFAGH VHAYERSERV 

       370        380        390        400        410        420 
SNVAYNIVNG LCAPVNDKSA PVYITIGDGG TLEGLATNMT EPQPKYSAFR EASFGHAIFD 

       430        440        450        460 
ITNRTHAHYS WHRNQDGVAV EADSLWSFNR YWHPVDDSTA HVSH

« Hide

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References

[1]"Binuclear metal centers in plant purple acid phosphatases: Fe-Mn in sweet potato and Fe-Zn in soybean."
Schenk G., Ge Y., Carrington L.E., Wynne C.J., Searle I.R., Carroll B.J., Hamilton S., de Jersey J.
Arch. Biochem. Biophys. 370:183-189(1999) [PubMed: 10510276] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: cv. Provar.
[2]"Purification and characterization of a secreted purple phosphatase from soybean suspension cultures."
Lebansky B.R., McKnight T.D., Griffing L.R.
Plant Physiol. 99:391-395(1992) [PubMed: 16668896] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-47, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF200824 mRNA. Translation: AAF19820.1.
PIRB59200.

3D structure databases

SMRQ09131. Positions 37-459.
ModBaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15155.
BRENDA3.1.3.2. 299.

Gene expression databases

GenevestigatorQ09131.

Family and domain databases

InterProIPR004843. M-pesterase.
IPR008963. Purple_acid_Pase-like_N.
IPR015914. Purple_acid_Pase_N.
[Graphical view]
Gene3DG3DSA:2.60.40.380. Purple_acid_Pase_N. 1 hit.
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePPAF_SOYBN
AccessionPrimary (citable) accession number: Q09131
Secondary accession number(s): Q9SE01
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: February 9, 2010
This is version 45 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents